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TitleCoat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions.
Journal, issue, pagesNat Struct Biol, Vol. 10, Issue 2, Page 131-135, Year 2003
Publish dateFeb 25, 2003
AuthorsWen Jiang / Zongli Li / Zhixian Zhang / Matthew L Baker / Peter E Prevelige / Wah Chiu /
PubMed AbstractBacteriophage P22 is a prototypical biological machine used for studying protein complex assembly and capsid maturation. Using cryo-EM, we solved the structures of P22 before and after the capsid ...Bacteriophage P22 is a prototypical biological machine used for studying protein complex assembly and capsid maturation. Using cryo-EM, we solved the structures of P22 before and after the capsid maturation at 8.5 A and 9.5 A resolutions, respectively. These structures allowed visualization of alpha-helices and beta-sheets from which the capsid protein fold is derived. The capsid fold is similar to that of the coat protein of HK97 bacteriophage. The cryo-EM shows that a large conformational change of the P22 capsid during maturation transition involves not only the domain movement of individual subunits, but also refolding of the capsid protein.
External linksNat Struct Biol / PubMed:12536205
MethodsEM (single particle)
Resolution9.5 Å
Structure data

EMDB-1101:
Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions.
Method: EM (single particle) / Resolution: 9.5 Å

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